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SMTN_MOUSE
ID   SMTN_MOUSE              Reviewed;         923 AA.
AC   Q921U8; Q3TCV2; Q6NSW1; Q8CD93; Q9JHG8; Q9JLU7; Q9R0D0; Q9R253; Q9Z0Q2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Smoothelin;
GN   Name=Smtn; Synonyms=Smsmo;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=L129;
RX   PubMed=10965129; DOI=10.1159/000015619;
RA   Rensen S., Merkx G., Doevendans P., Geurts Van Kessel A., van Eys G.J.J.M.;
RT   "Structure and chromosome location of Smtn, the mouse smoothelin gene.";
RL   Cytogenet. Cell Genet. 89:225-229(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS L1 AND L2).
RC   STRAIN=129; TISSUE=Heart;
RX   PubMed=10023782; DOI=10.1007/s001090050352;
RA   Kraemer J., Aguirre-Arteta A.M., Thiel C., Gross M.C., Dietz R.,
RA   Cardoso M.C., Leonhardt H.;
RT   "A novel isoform of the smooth muscle cell differentiation marker
RT   smoothelin.";
RL   J. Mol. Med. 77:294-298(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=129;
RA   Kraemer J., Cardoso M.C., Gross C.M., Dietz R., Leonhardt H.;
RT   "Mouse smoothelin gene structure and its splicing variants.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM L2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM L2).
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Blastocyst, Embryo, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Heart, and Kidney;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Structural protein of the cytoskeleton. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC       Note=Exhibits a filamentous organization. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=L1; Synonyms=B;
CC         IsoId=Q921U8-1; Sequence=Displayed;
CC       Name=L2;
CC         IsoId=Q921U8-2; Sequence=VSP_031244;
CC       Name=S1; Synonyms=A;
CC         IsoId=Q921U8-3; Sequence=VSP_031243;
CC       Name=S2;
CC         IsoId=Q921U8-4; Sequence=VSP_031243, VSP_031244;
CC   -!- SIMILARITY: Belongs to the smoothelin family. {ECO:0000305}.
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DR   EMBL; AF218834; AAD29628.2; -; Genomic_DNA.
DR   EMBL; AF116517; AAD29628.2; JOINED; Genomic_DNA.
DR   EMBL; AF116518; AAD29628.2; JOINED; Genomic_DNA.
DR   EMBL; AF195524; AAD29628.2; JOINED; Genomic_DNA.
DR   EMBL; AF195525; AAD29628.2; JOINED; Genomic_DNA.
DR   EMBL; AF218829; AAD29628.2; JOINED; Genomic_DNA.
DR   EMBL; AF218830; AAD29628.2; JOINED; Genomic_DNA.
DR   EMBL; AF218831; AAD29628.2; JOINED; Genomic_DNA.
DR   EMBL; AF218832; AAD29628.2; JOINED; Genomic_DNA.
DR   EMBL; AF218833; AAD29628.2; JOINED; Genomic_DNA.
DR   EMBL; AF218834; AAF67392.1; -; Genomic_DNA.
DR   EMBL; AF116518; AAF67392.1; JOINED; Genomic_DNA.
DR   EMBL; AF195525; AAF67392.1; JOINED; Genomic_DNA.
DR   EMBL; AF218830; AAF67392.1; JOINED; Genomic_DNA.
DR   EMBL; AF218831; AAF67392.1; JOINED; Genomic_DNA.
DR   EMBL; AF218832; AAF67392.1; JOINED; Genomic_DNA.
DR   EMBL; AF218833; AAF67392.1; JOINED; Genomic_DNA.
DR   EMBL; AF064236; AAF01480.1; -; mRNA.
DR   EMBL; AJ010305; CAA09076.1; -; mRNA.
DR   EMBL; AF132449; AAF25577.2; -; Genomic_DNA.
DR   EMBL; AF132449; AAF25578.2; -; Genomic_DNA.
DR   EMBL; AF132449; AAF25579.2; -; Genomic_DNA.
DR   EMBL; AF132449; AAF25580.2; -; Genomic_DNA.
DR   EMBL; AK030932; BAC27188.1; -; mRNA.
DR   EMBL; AK170516; BAE41853.1; -; mRNA.
DR   EMBL; BC010599; AAH10599.1; -; mRNA.
DR   EMBL; BC066192; AAH66192.1; -; mRNA.
DR   EMBL; BC069836; AAH69836.1; -; mRNA.
DR   EMBL; BC069839; AAH69839.1; -; mRNA.
DR   CCDS; CCDS24366.1; -. [Q921U8-2]
DR   CCDS; CCDS70129.1; -. [Q921U8-1]
DR   RefSeq; NP_001152756.1; NM_001159284.1. [Q921U8-2]
DR   RefSeq; NP_001271356.1; NM_001284427.1. [Q921U8-1]
DR   RefSeq; NP_001271357.1; NM_001284428.1. [Q921U8-2]
DR   RefSeq; NP_001271358.1; NM_001284429.1.
DR   RefSeq; NP_038898.2; NM_013870.3. [Q921U8-2]
DR   RefSeq; XP_017170075.1; XM_017314586.1. [Q921U8-1]
DR   AlphaFoldDB; Q921U8; -.
DR   SMR; Q921U8; -.
DR   BioGRID; 205923; 4.
DR   IntAct; Q921U8; 2.
DR   STRING; 10090.ENSMUSP00000020721; -.
DR   iPTMnet; Q921U8; -.
DR   PhosphoSitePlus; Q921U8; -.
DR   EPD; Q921U8; -.
DR   MaxQB; Q921U8; -.
DR   PaxDb; Q921U8; -.
DR   PeptideAtlas; Q921U8; -.
DR   PRIDE; Q921U8; -.
DR   ProteomicsDB; 261378; -. [Q921U8-1]
DR   ProteomicsDB; 261379; -. [Q921U8-2]
DR   ProteomicsDB; 261380; -. [Q921U8-3]
DR   ProteomicsDB; 261381; -. [Q921U8-4]
DR   Antibodypedia; 3445; 177 antibodies from 24 providers.
DR   DNASU; 29856; -.
DR   Ensembl; ENSMUST00000020721; ENSMUSP00000020721; ENSMUSG00000020439. [Q921U8-2]
DR   Ensembl; ENSMUST00000075118; ENSMUSP00000074621; ENSMUSG00000020439. [Q921U8-1]
DR   Ensembl; ENSMUST00000170588; ENSMUSP00000133155; ENSMUSG00000020439. [Q921U8-2]
DR   GeneID; 29856; -.
DR   KEGG; mmu:29856; -.
DR   UCSC; uc007htf.2; mouse. [Q921U8-2]
DR   UCSC; uc007hti.2; mouse. [Q921U8-1]
DR   CTD; 6525; -.
DR   MGI; MGI:1354727; Smtn.
DR   VEuPathDB; HostDB:ENSMUSG00000020439; -.
DR   eggNOG; KOG4678; Eukaryota.
DR   GeneTree; ENSGT00940000161655; -.
DR   HOGENOM; CLU_014660_0_0_1; -.
DR   InParanoid; Q921U8; -.
DR   OMA; KTPYPGF; -.
DR   OrthoDB; 168604at2759; -.
DR   TreeFam; TF316716; -.
DR   BioGRID-ORCS; 29856; 4 hits in 71 CRISPR screens.
DR   ChiTaRS; Smtn; mouse.
DR   PRO; PR:Q921U8; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q921U8; protein.
DR   Bgee; ENSMUSG00000020439; Expressed in aorta tunica media and 167 other tissues.
DR   ExpressionAtlas; Q921U8; baseline and differential.
DR   Genevisible; Q921U8; MM.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0031941; C:filamentous actin; IBA:GO_Central.
DR   GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR   GO; GO:0003779; F:actin binding; TAS:MGI.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; IMP:MGI.
DR   GO; GO:0060452; P:positive regulation of cardiac muscle contraction; IMP:MGI.
DR   CDD; cd00014; CH; 1.
DR   Gene3D; 1.10.418.10; -; 1.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR022189; SMTN.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF12510; Smoothelin; 3.
DR   SMART; SM00033; CH; 1.
DR   SUPFAM; SSF47576; SSF47576; 1.
DR   PROSITE; PS50021; CH; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P53814"
FT   CHAIN           2..923
FT                   /note="Smoothelin"
FT                   /id="PRO_0000318593"
FT   DOMAIN          805..912
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   REGION          134..456
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          542..578
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          615..772
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          24..89
FT                   /evidence="ECO:0000255"
FT   COILED          601..628
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        161..188
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        237..253
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        276..322
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        363..389
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        615..637
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        640..724
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        744..758
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P53814"
FT   MOD_RES         299
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53814"
FT   MOD_RES         301
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53814"
FT   MOD_RES         304
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53814"
FT   MOD_RES         340
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53814"
FT   MOD_RES         359
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P53814"
FT   MOD_RES         372
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P53814"
FT   MOD_RES         501
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53814"
FT   MOD_RES         521
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53814"
FT   MOD_RES         574
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53814"
FT   MOD_RES         641
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         735
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53814"
FT   MOD_RES         798
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53814"
FT   VAR_SEQ         1..454
FT                   /note="Missing (in isoform S1 and isoform S2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_031243"
FT   VAR_SEQ         875..923
FT                   /note="MLVDCVPLVEVEDMMIMGKKPDPKCVFTYVQSLYNHLRRHELRLRGKNV ->
FT                   THADCPQLLDTEDMVRLREPDWKCVYTYIQEFYRCLVQKGLVKTKKS (in isoform
FT                   L2 and isoform S2)"
FT                   /evidence="ECO:0000303|PubMed:10023782,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT                   /id="VSP_031244"
FT   CONFLICT        173
FT                   /note="P -> S (in Ref. 1; AAD29628, 2; AAF01480/CAA09076
FT                   and 3; AAF25577/AAF25578)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        379
FT                   /note="Missing (in Ref. 5; AAH69839/AAH69836/AAH66192)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        441
FT                   /note="P -> Q (in Ref. 4; BAE41853)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        448
FT                   /note="T -> N (in Ref. 4; BAC27188)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        450
FT                   /note="E -> G (in Ref. 5; AAH69839/AAH69836/AAH66192)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        711
FT                   /note="S -> N (in Ref. 1; AAD29628/AAF67392, 2; AAF01480/
FT                   CAA09076 and 3; AAF25577/AAF25578/AAF25579/AAF25580)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        756
FT                   /note="M -> V (in Ref. 5; AAH69839/AAH69836/AAH66192)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        837
FT                   /note="G -> R (in Ref. 1; AAD29628/AAF67392, 2; AAF01480/
FT                   CAA09076 and 3; AAF25577/AAF25578/AAF25579/AAF25580)"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         Q921U8-2:372
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   923 AA;  100289 MW;  2E70E413C8B487C7 CRC64;
     MADEALAGLD EGALRKLLEV TADLAERRRI RSAIRELQRQ ELEREEEALA SKRFRAERQD
     NKENWLHSQQ REAEQQAALA RLAGRLESMN DVEELTTLLR SAGEYEERKL IRAAIRRVRA
     QEIKAATLAG RLCSRLPSSG PREDSRRQAA HTLDPGKVPE PEQQEQQTEV LEPTPTPEDT
     SQDVTTVTLL LRAPPGGRPS SPASPHNSPT SASPEPLLEP AGAQCPAVEA PVSSEPLPHP
     SEAPSPEPPM SPVPSSSRGR VISKPLPGPT EPSDTLDSIR GFSNTKRADP SETKSCQRSL
     SVLSPRQPTP NREPTSLAGP SQFRRVGSVR DRVQKFTSDS PVVARLQDGP PRTALASPTP
     TRLPGPSLIS TTPASSSSSN SSSPSPSDTS SHKKQRELAH SLAELQSCPQ EEGPGGRGLA
     LRSLENRAGG PKPCSEEPST PPPVAVGTGE PGGSMKTTFT IEIKDGRGQA STGRVLLPTG
     NQRAELTLGL RAPPTLLSTS SGGKNTITHI SNPGTVTRLG SVTHVTTFSH ASPGNRGGCN
     FKMEPDPAEP PSTTVEAANG AEQARVDKGP EGRSPLSAEE LTAIEDEGVL DKMLDQTTNF
     EERKLIRAAL RELRQRKRDQ RDKERERRLR EARARPGESR SNVATETTTR HSQRAADGST
     VGTVTKTERL VHSNDGTQTA RTTTVESSFM RRLENGSSSS STTTTTVQTK SFSSSSSSSS
     SKKMGSIFDR EDQTSSRPGS LAALERRQAE KKKELMKAQS LPKTSASQAR KAMIEKLEKE
     GSAGGPGTPR TAVQRSTSFG VPNANSIKQM LLDWCRAKTR GYEHVDIQNF SSSWSDGMAF
     CALVHNFFPE AFDYGQLSPQ NRRQNFEMAF SSAEMLVDCV PLVEVEDMMI MGKKPDPKCV
     FTYVQSLYNH LRRHELRLRG KNV
 
 
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